Phosphogluconate Dehydrogenase (PGD)

Phosphogluconate dehydrogenase (PGD), also known as 6-PGD, 6PGDH, is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. 6-PGD protein was absent from the oxidase complex isolated from B lymphocytes, suggesting a specific interaction with the neutrophil NADPH oxidase. PGD/6PGDH constitutes the pentose phosphate pathway and produces NADPH. 6PGDH is also considered as a lipogenic gene since NADPH is a pivotal cofactor for lipogenesis. 6PGDH mRNA is highly expressed in white adipose tissue and tightly modulated by nutritional status. Furthermore, ADD1/SREBP1c mediates insulin-dependent 6PGDH expression and that PI3-kinase is an important linker for its regulation.

Phosphogluconate Dehydrogenase (PGD) Alternative Names

PGD, Phosphogluconate dehydrogenase, 6PGD [Homo sapiens]

PGD, Phosphogluconate dehydrogenase, Pgd,RP23-249G3.4, 0610042A05Rik, AU019875, C78335 [Mus musculus]

Summaries for Phosphogluconate Dehydrogenase (PGD)

Entrez Gene summary for Phosphogluconate Dehydrogenase (PGD):

6-phosphogluconate dehydrogenase is the second dehydrogenase in the pentose phosphate shunt. Deficiency of this enzyme is generally asymptomatic, and the inheritance of this disorder is autosomal dominant. Hemolysis results from combined deficiency of 6-phosphogluconate dehydrogenase and 6-phosphogluconolactonase suggesting a synergism of the two enzymopathies. [provided by RefSeq, Jul 2008]

Wikipedia summary for Phosphogluconate Dehydrogenase (PGD):

Phosphogluconate dehydrogenase is an enzyme in the pentose phosphate pathway. It forms ribulose 5-phosphate from 6-phosphogluconate.
It is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP). Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved. The protein is a homodimer in which the monomers act independently : each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet. NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket.

Human Phosphogluconate Dehydrogenase (PGD) Protein General Information

 

• Protein names: 6-phosphogluconate dehydrogenase, decarboxylating
  Short name=PGD
• Sequence length: 483 AA.
• Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.
• Sequence similarities: Belongs to the 6-phosphogluconate dehydrogenase family.
• Catalytic activity: 6-phospho-D-gluconate + NADP⁺ = D-ribulose 5-phosphate + CO₂ + NADPH.
• Subunit structure: Homodimer.
• Subcellular location: Cytoplasm

General information above from UniProt

Function for Phosphogluconate Dehydrogenase (PGD) Protein

UniProtKB:

Phosphogluconate dehydrogenase catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.

Genatlas:

• Phosphogluconate dehydrogenase is second dehydrogenase in the pentose phosphate shunt